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Volumn 415, Issue 1, 2003, Pages 80-86
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Proteolytic cleavage of the puromycin-sensitive aminopeptidase generates a substrate binding domain
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Author keywords
Domain structure; Peptidase; Protein folding; Substrate binding
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Indexed keywords
AMINOPEPTIDASE;
ARGININE 2 NAPHTHYLAMIDE;
ARGININE DERIVATIVE;
CHYMOTRYPSIN;
DYNORPHIN B;
DYNORPHIN[1-9];
GLYCYLGLYCYLPHENYLALANYLLEUCINE;
HISTIDINE;
HYBRID PROTEIN;
PROTEINASE;
PROTEINASE K;
PUROMYCIN SENSITIVE AMINOPEPTIDASE;
TRYPSIN;
UNCLASSIFIED DRUG;
UREA;
AMINO ACID SEQUENCE;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING SITE;
CARBOXY TERMINAL SEQUENCE;
CELL INCLUSION;
CONTROLLED STUDY;
DIALYSIS;
ENZYME ACTIVITY;
ENZYME ASSAY;
ENZYME BINDING;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
INHIBITION KINETICS;
MOLECULAR WEIGHT;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DEGRADATION;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN FOLDING;
PROTEIN FUNCTION;
SOLUBILIZATION;
ESCHERICHIA COLI;
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EID: 0037834880
PISSN: 00039861
EISSN: None
Source Type: Journal
DOI: 10.1016/S0003-9861(03)00200-5 Document Type: Article |
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Times cited : (8)
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References (17)
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